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Evidence for α-1,6 and α-1,4-glucosidic bond cleavage in highly branched glycogen by amylopullulanase from Thermoanaerobacter ethanolicus

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Summary

Activity of amylopullulanase from Thermoanaerobacter ethanolicus 39E on α-1,6 and α-1,4-glucosidic linkages in highly branched mammalian glycogen was analyzed by paper chromatography and 13C nuclear magnetic resonance (NMR) spectroscopy. Paper chromatography analysis showed that the glycogen hydrolysate consisted of glucose, maltose, maltotriose and maltotetraose. NMR spectroscopy confirmed that no hydrolysate products of α-1,6 linkage were present resulting from treatment with the amylopullulanase. Therefore, the amylopullulanase efficiently hydrolyzed glycogen both at α-1,6- and at α-1,4-glucosidic linkages into oligosaccharides.

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Authors and Affiliations

  1. Department of Biochemistry, Michigan State University, 48824, East Lansing, MI, USA

    Saroj P. Mathupala, Jong-Hyun Park & J. Gregory Zeikus

  2. Michigan Biotechnology Institute, 48909, Lansing, MI, USA

    J. Gregory Zeikus

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  1. Saroj P. Mathupala
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  2. Jong-Hyun Park
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  3. J. Gregory Zeikus
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Mathupala, S.P., Park, JH. & Zeikus, J.G. Evidence for α-1,6 and α-1,4-glucosidic bond cleavage in highly branched glycogen by amylopullulanase from Thermoanaerobacter ethanolicus . Biotechnol Lett 16, 1311–1316 (1994). https://doi.org/10.1007/BF00149638

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  • DOI: https://doi.org/10.1007/BF00149638

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